MG_453_MONOMER – UTP-glucose-1-phosphate uridylyltransferase

Name
WID MG_453_MONOMER View in model
Name UTP-glucose-1-phosphate uridylyltransferase View in model
Cross references PDB: 2E3D
 
Genetics
Gene MG_453 View in model
 
Structure
Sequence
1
51
101
151
201
251
MKTKIRKAVIPAAGLGVRLLPATKAIPKEMLPLVNKPTIQYIVEEAVKSG
IEQILVIVSSKKTAILDHFDYDLILENALIQKNKLQEHKEIEDIANLAHI
FFVRQKNQDGLGDAILFAESFVGNEDFAVLLGDDVVFSKEPALKQCLEAY
YETNCQTIGVQEVDPCHVDKYGIITPEGDYKNKDLIKVLAMTEKPKPKDA
KSNLAILGRYVLKPSIFKALRSVPYGVGGELQLTDGLNFCLKNENFYARK
FTGTRFDVGTKSGFIKANLFTALNNKDISKKEVLELLNLVKA*
50
100
150
200
250
293
View in model
Is N‑terminal methionine cleaved
No
View in model
Prosthetic groups View in model
Empirical formula (pH 7.5) H2385C1480N380O425S7
Molecular weight (pH 7.5; Da) 32526.42 View in model
Extinction coefficient 
(260 nm, 25C, pH 7.0)
13910
Instability index 33.70
Is stable True
Aliphatic index 105.49
GRAVY (25C, pH 7.0) -0.0932
Half life (OD (600 nm) = 0.3, 
M9 media, 36C; min)
1200 View in model
 
Synthesis
Localization c View in model
 
Function
Complex subunit UTP-glucose-1-phosphate uridylyltransferase
[c]: (4) MG_453_MONOMERMG_453_TETRAMER
View in model
 
Comments
Comments Functional Macromolecule Homologous to E. coli galU. E. coli GalF is a structural protein which stabilizes GalU and increases its enzymatic activity [PUB_0426]. Alone GalU is enzymatically active. M. genitalium appears to have only a GalU homolog. GalU is functional as homotetramer. Coenzymes Monomer interacts with MG with unknown stoichiometry as prosthetic group.
References
  1. Marolda CL, Valvano MA. The GalF protein of Escherichia coli is not a UDP-glucose pyrophosphorylase but interacts with the GalU protein possibly to regulate cellular levels of UDP-glucose. Mol Microbiol 22, 827-40 (1996). WholeCell: PUB_0426, PubMed: 8971705

 
Metadata
Created 2012-10-01 15:08:03
Last updated 2012-10-01 15:14:51